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  • 1.
    Ndi, Mama
    et al.
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Masuyer, Geoffrey
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. University of Bath, UK.
    Dawitz, Hannah
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Carlström, Andreas
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Michel, Mirco
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. Stockholm University, Science for Life Laboratory (SciLifeLab).
    Elofsson, Arne
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. Stockholm University, Science for Life Laboratory (SciLifeLab).
    Rapp, Mikaela
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Stenmark, Pål
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. Lund University, Sweden.
    Ott, Martin
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Structural basis for Cbp3 interaction with newly synthesized cytochrome b during mitochondrial respiratory chain assembly2019In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 294, no 45, p. 16663-16671Article in journal (Refereed)
    Abstract [en]

    Assembly of the mitochondrial respiratory chain requires the coordinated synthesis of mitochondrial and nuclear encoded subunits, redox co-factor acquisition, and correct joining of the subunits to form functional complexes. The conserved Cbp3–Cbp6 chaperone complex binds newly synthesized cytochrome b and supports the ordered acquisition of the heme co-factors. Moreover, it functions as a translational activator by interacting with the mitoribosome. Cbp3 consists of two distinct domains, an N-terminal domain present in mitochondrial Cbp3 homologs, and a highly conserved C-terminal domain comprising a ubiquinol–cytochrome c chaperone region. Here, we solved the crystal structure of this C-terminal domain from a bacterial homolog at 1.4 Å resolution, revealing a unique all-helical fold. This structure allowed mapping of the interaction sites of yeast Cbp3 with Cbp6 and cytochrome b via site-specific photo-crosslinking. We propose that mitochondrial Cbp3 homologs carry an N-terminal extension that positions the conserved C-terminal domain at the ribosomal tunnel exit for an efficient interaction with its substrate, the newly synthesized cytochrome b protein.

  • 2.
    Singh, Abeer Prakash
    et al.
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Salvatori, Roger
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Aftab, Wasim
    Carlström, Andreas
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Forne, Ignasi
    Imhof, Axel
    Ott, Martin
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    A protein proximity atlas reveals connectivity of mitochondrial translation and OXPHOS assembly at the ribosomal tunnel exitManuscript (preprint) (Other academic)
  • 3.
    Vargas Möller-Hergt, Braulio
    et al.
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Carlström, Andreas
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Stephan, Katharina
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Imhof, Axel
    Ott, Martin
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    The ribosome receptors Mrx15 and Mba1 jointly organize cotranslational insertion and protein biogenesis in mitochondria2018In: Molecular Biology of the Cell, ISSN 1059-1524, E-ISSN 1939-4586, Vol. 29, no 20, p. 2359-2507Article in journal (Refereed)
    Abstract [en]

    Mitochondrial gene expression in Saccharomyces cerevisiae is responsible for the production of highly hydrophobic subunits of the oxidative phosphorylation system. Membrane insertion occurs cotranslationally on membrane-bound mitochondrial ribosomes. Here, by employing a systematic mass spectrometry-based approach, we discovered the previously uncharacterized membrane protein Mrx15 that interacts via a soluble C-terminal domain with the large ribosomal subunit. Mrx15 contacts mitochondrial translation products during their synthesis and plays, together with the ribosome receptor Mba1, an overlapping role in cotranslational protein insertion. Taken together, our data reveal how these ribosome receptors organize membrane protein biogenesis in mitochondria.

  • 4.
    Vargas Möller-Hergt, Braulio
    et al.
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Carlström, Andreas
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Suhm, Tamara
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Ott, Martin
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Insertion Defects of Mitochondrially Encoded Proteins Burden the Mitochondrial Quality Control System2018In: Cells, ISSN 2073-4409, Vol. 7, no 10, article id 172Article in journal (Refereed)
    Abstract [en]

    The mitochondrial proteome contains proteins from two different genetic systems. Proteins are either synthesized in the cytosol and imported into the different compartments of the organelle or directly produced in the mitochondrial matrix. To ensure proteostasis, proteins are monitored by the mitochondrial quality control system, which will degrade non-native polypeptides. Defective mitochondrial membrane proteins are degraded by membrane-bound AAA-proteases. These proteases are regulated by factors promoting protein turnover or preventing their degradation. Here we determined genetic interactions between the mitoribosome receptors Mrx15 and Mba1 with the quality control system. We show that simultaneous absence of Mrx15 and the regulators of the i-AAA protease Mgr1 and Mgr3 provokes respiratory deficiency. Surprisingly, mutants lacking Mrx15 were more tolerant against proteotoxic stress. Furthermore, yeast cells became hypersensitive against proteotoxic stress upon deletion of MBA1. Contrary to Mrx15, Mba1 cooperates with the regulators of the m-AAA and i-AAA proteases. Taken together, these results suggest that membrane protein insertion and mitochondrial AAA-proteases are functionally coupled, possibly reflecting an early quality control step during mitochondrial protein synthesis.

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